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          Institute: MPI für molekulare Genetik     Collection: Microscopy     Display Documents



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ID: 412055.0, MPI für molekulare Genetik / Microscopy
Origin and function of the two major tail proteins of bacteriophage SPP1
Authors:Auzat, Isabelle; Dröge, Anja; Weise, Frank; Lurz, Rudi; Tavares, Paulo
Language:English
Date of Publication (YYYY-MM-DD):2008-09-10
Title of Journal:Molecular Microbiology
Journal Abbrev.:Mol Micro
Volume:70
Issue / Number:3
Start Page:557
End Page:569
Copyright:© 2008 Blackwell Publishing
Review Status:not specified
Audience:Experts Only
Abstract / Description:The majority of bacteriophages have a long non-contractile tail (Siphoviridae) that serves as a conduit for viral DNA traffic from the phage capsid to the host cell at the beginning of infection. The 160-nm-long tail tube of Bacillus subtilis bacteriophage SPP1 is shown to be composed of two major tail proteins (MTPs), gp17.1 and gp17.1*, at a ratio of about 3:1. They share a common amino-terminus, but the latter species has ∼10 kDa more than gp17.1. A CCC.UAA sequence with overlapping proline codons at the 3' end of gene 17.1 drives a programmed translational frameshift to another open reading frame. The recoding event generates gp17.1*. Phages carrying exclusively gp17.1 or gp17.1* are viable, but tails are structurally distinct. gp17.1 and the carboxyl-terminus of gp17.1* have a distinct evolutionary history correlating with different functions: the polypeptide sequence identical in the two proteins is responsible for assembly of the tail tube while the additional module of gp17.1* shields the structure exterior exposed to the environment. The carboxyl-terminal extension is an elaboration present in some tailed bacteriophages. Different extensions were found to combine in a mosaic fashion with the MTP essential module in a subset of Siphoviridae genomes.
External Publication Status:published
Document Type:Article
Communicated by:Rudi Lurz
Affiliations:MPI für molekulare Genetik
External Affiliations:1.Unité de Virologie Moléculaire et Structurale, CNRS UMR 2472, INRA UMR1157 and IFR 115, Bâtiment 14B, CNRS, 91198 Gif-sur-Yvette, France.
Identifiers:URL:http://www3.interscience.wiley.com/cgi-bin/fulltex...
DOI:10.1111/j.1365-2958.2008.06435.x
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